LFNG_HUMAN
ID LFNG_HUMAN Reviewed; 379 AA.
AC Q8NES3; B3KTY6; B5MCR5; O00589; Q96C39; Q9UJW5;
DT 10-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe;
DE EC=2.4.1.222;
DE AltName: Full=O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase;
GN Name=LFNG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 105-361 (ISOFORM 3).
RX PubMed=9187150; DOI=10.1242/dev.124.11.2245;
RA Johnston S.H., Rauskolb C., Wilson R., Prabhakaran B., Irvine K.D.,
RA Vogt T.F.;
RT "A family of mammalian Fringe genes implicated in boundary determination
RT and the Notch pathway.";
RL Development 124:2245-2254(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-144 (ISOFORM 1).
RX PubMed=12110169; DOI=10.1016/s1534-5807(02)00212-5;
RA Cole S.E., Levorse J.M., Tilghman S.M., Vogt T.F.;
RT "Clock regulatory elements control cyclic expression of Lunatic fringe
RT during somitogenesis.";
RL Dev. Cell 3:75-84(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 104-361 (ISOFORM 3).
RA Holloway J., Blumberg H., Jelinek L., Whitmore T., Jaspers S., Gross J.,
RA Haldeman B., Taft D., O'Hara P.;
RT "Homo sapiens fringe gene homolog.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP FUNCTION.
RX PubMed=11346656; DOI=10.1074/jbc.m103473200;
RA Shimizu K., Chiba S., Saito T., Kumano K., Takahashi T., Hirai H.;
RT "Manic fringe and lunatic fringe modify different sites of the Notch2
RT extracellular region, resulting in different signaling modulation.";
RL J. Biol. Chem. 276:25753-25758(2001).
RN [8]
RP VARIANT SCDO3 LEU-188, AND CHARACTERIZATION OF VARIANT SCDO3 LEU-188.
RX PubMed=16385447; DOI=10.1086/498879;
RA Sparrow D.B., Chapman G., Wouters M.A., Whittock N.V., Ellard S.,
RA Fatkin D., Turnpenny P.D., Kusumi K., Sillence D., Dunwoodie S.L.;
RT "Mutation of the LUNATIC FRINGE gene in humans causes spondylocostal
RT dysostosis with a severe vertebral phenotype.";
RL Am. J. Hum. Genet. 78:28-37(2006).
RN [9]
RP VARIANTS ARG-38 AND MET-346.
RX PubMed=18485326; DOI=10.1016/j.ajhg.2008.04.014;
RA Cornier A.S., Staehling-Hampton K., Delventhal K.M., Saga Y., Caubet J.-F.,
RA Sasaki N., Ellard S., Young E., Ramirez N., Carlo S.E., Torres J.,
RA Emans J.B., Turnpenny P.D., Pourquie O.;
RT "Mutations in the MESP2 gene cause spondylothoracic dysostosis/Jarcho-Levin
RT syndrome.";
RL Am. J. Hum. Genet. 82:1334-1341(2008).
CC -!- FUNCTION: Glycosyltransferase that initiates the elongation of O-linked
CC fucose residues attached to EGF-like repeats in the extracellular
CC domain of Notch molecules. Modulates NOTCH1 activity by modifying O-
CC fucose residues at specific EGF-like domains resulting in inhibition of
CC NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1
CC via an increase in its binding to DLL1 (By similarity). Decreases the
CC binding of JAG1 to NOTCH2 but not that of DLL1 (PubMed:11346656).
CC Essential mediator of somite segmentation and patterning (By
CC similarity). {ECO:0000250|UniProtKB:O09010,
CC ECO:0000269|PubMed:11346656}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] +
CC UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-
CC (1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-
CC COMP:17923, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:189631, ChEBI:CHEBI:189634; EC=2.4.1.222;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3-O-(alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + UDP-
CC N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-
CC (1->3)-alpha-L-fucosyl)-L-seryl-[EGF-like domain protein] + H(+) +
CC UDP; Xref=Rhea:RHEA:70511, Rhea:RHEA-COMP:17919, Rhea:RHEA-
CC COMP:17920, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:189632, ChEBI:CHEBI:189633; EC=2.4.1.222;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-
CC pass type II membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Comment=Experimental confirmation may be lacking for some isoforms.;
CC Name=1;
CC IsoId=Q8NES3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NES3-2; Sequence=VSP_001792, VSP_001793;
CC Name=3;
CC IsoId=Q8NES3-3; Sequence=VSP_001794, VSP_001795;
CC Name=4;
CC IsoId=Q8NES3-4; Sequence=VSP_044850, VSP_044851;
CC -!- PTM: A soluble form may be derived from the membrane form by
CC proteolytic processing. {ECO:0000305}.
CC -!- DISEASE: Spondylocostal dysostosis 3, autosomal recessive (SCDO3)
CC [MIM:609813]: A condition of variable severity associated with
CC vertebral and rib segmentation defects. The main skeletal malformations
CC include fusion of vertebrae, hemivertebrae, fusion of certain ribs, and
CC other rib malformations. Deformity of the chest and spine (severe
CC scoliosis, kyphoscoliosis and lordosis) is a natural consequence of the
CC malformation and leads to a dwarf-like appearance. As the thorax is
CC small, infants frequently have respiratory insufficiency and repeated
CC respiratory infections resulting in life-threatening complications in
CC the first year of life. {ECO:0000269|PubMed:16385447}. Note=The disease
CC is caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 31 family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=Beta-1,3-
CC N-acetylglucosaminyltransferase lunatic fringe;
CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_551";
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DR EMBL; AK096284; BAG53248.1; -; mRNA.
DR EMBL; AC092488; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U94354; AAC51360.1; -; mRNA.
DR EMBL; AY124582; AAM93542.1; -; Genomic_DNA.
DR EMBL; AF193612; AAF07187.1; -; mRNA.
DR EMBL; BC014851; AAH14851.1; -; mRNA.
DR CCDS; CCDS34586.1; -. [Q8NES3-3]
DR CCDS; CCDS34587.1; -. [Q8NES3-1]
DR CCDS; CCDS55081.1; -. [Q8NES3-4]
DR CCDS; CCDS55082.1; -. [Q8NES3-2]
DR RefSeq; NP_001035257.1; NM_001040167.1. [Q8NES3-1]
DR RefSeq; NP_001035258.1; NM_001040168.1. [Q8NES3-3]
DR RefSeq; NP_001159827.1; NM_001166355.1. [Q8NES3-4]
DR RefSeq; NP_002295.1; NM_002304.2. [Q8NES3-2]
DR AlphaFoldDB; Q8NES3; -.
DR SMR; Q8NES3; -.
DR BioGRID; 110146; 12.
DR STRING; 9606.ENSP00000222725; -.
DR CAZy; GT31; Glycosyltransferase Family 31.
DR GlyConnect; 1031; 1 N-Linked glycan (1 site).
DR GlyGen; Q8NES3; 1 site, 1 N-linked glycan (1 site).
DR iPTMnet; Q8NES3; -.
DR PhosphoSitePlus; Q8NES3; -.
DR BioMuta; LFNG; -.
DR DMDM; 27734417; -.
DR EPD; Q8NES3; -.
DR jPOST; Q8NES3; -.
DR MassIVE; Q8NES3; -.
DR MaxQB; Q8NES3; -.
DR PaxDb; Q8NES3; -.
DR PeptideAtlas; Q8NES3; -.
DR PRIDE; Q8NES3; -.
DR ProteomicsDB; 6090; -.
DR ProteomicsDB; 73208; -. [Q8NES3-1]
DR ProteomicsDB; 73209; -. [Q8NES3-2]
DR ProteomicsDB; 73210; -. [Q8NES3-3]
DR Antibodypedia; 24378; 329 antibodies from 32 providers.
DR DNASU; 3955; -.
DR Ensembl; ENST00000222725.10; ENSP00000222725.5; ENSG00000106003.14. [Q8NES3-1]
DR Ensembl; ENST00000338732.7; ENSP00000343095.3; ENSG00000106003.14. [Q8NES3-2]
DR Ensembl; ENST00000359574.7; ENSP00000352579.3; ENSG00000106003.14. [Q8NES3-3]
DR Ensembl; ENST00000402045.5; ENSP00000384786.1; ENSG00000106003.14. [Q8NES3-2]
DR Ensembl; ENST00000402506.5; ENSP00000385764.1; ENSG00000106003.14. [Q8NES3-4]
DR GeneID; 3955; -.
DR KEGG; hsa:3955; -.
DR MANE-Select; ENST00000222725.10; ENSP00000222725.5; NM_001040167.2; NP_001035257.1.
DR UCSC; uc003smf.4; human. [Q8NES3-1]
DR CTD; 3955; -.
DR DisGeNET; 3955; -.
DR GeneCards; LFNG; -.
DR GeneReviews; LFNG; -.
DR HGNC; HGNC:6560; LFNG.
DR HPA; ENSG00000106003; Tissue enhanced (pancreas, skin).
DR MalaCards; LFNG; -.
DR MIM; 602576; gene.
DR MIM; 609813; phenotype.
DR neXtProt; NX_Q8NES3; -.
DR OpenTargets; ENSG00000106003; -.
DR Orphanet; 2311; Autosomal recessive spondylocostal dysostosis.
DR PharmGKB; PA30336; -.
DR VEuPathDB; HostDB:ENSG00000106003; -.
DR eggNOG; ENOG502QV30; Eukaryota.
DR GeneTree; ENSGT00940000158717; -.
DR HOGENOM; CLU_056611_1_0_1; -.
DR InParanoid; Q8NES3; -.
DR OMA; SENKMRP; -.
DR OrthoDB; 826272at2759; -.
DR PhylomeDB; Q8NES3; -.
DR TreeFam; TF324207; -.
DR BRENDA; 2.4.1.222; 2681.
DR PathwayCommons; Q8NES3; -.
DR Reactome; R-HSA-1912420; Pre-NOTCH Processing in Golgi.
DR Reactome; R-HSA-5083630; Defective LFNG causes SCDO3.
DR SignaLink; Q8NES3; -.
DR SIGNOR; Q8NES3; -.
DR BioGRID-ORCS; 3955; 14 hits in 1081 CRISPR screens.
DR ChiTaRS; LFNG; human.
DR GeneWiki; LFNG; -.
DR GenomeRNAi; 3955; -.
DR Pharos; Q8NES3; Tbio.
DR PRO; PR:Q8NES3; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q8NES3; protein.
DR Bgee; ENSG00000106003; Expressed in granulocyte and 93 other tissues.
DR ExpressionAtlas; Q8NES3; baseline and differential.
DR Genevisible; Q8NES3; HS.
DR GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
DR GO; GO:1903561; C:extracellular vesicle; HDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0030173; C:integral component of Golgi membrane; IEA:InterPro.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033829; F:O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity; IDA:FlyBase.
DR GO; GO:0009887; P:animal organ morphogenesis; NAS:UniProtKB.
DR GO; GO:0007386; P:compartment pattern specification; IEA:Ensembl.
DR GO; GO:0002315; P:marginal zone B cell differentiation; ISS:UniProtKB.
DR GO; GO:1902367; P:negative regulation of Notch signaling pathway involved in somitogenesis; ISS:UniProtKB.
DR GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
DR GO; GO:0051446; P:positive regulation of meiotic cell cycle; IEA:Ensembl.
DR GO; GO:0045747; P:positive regulation of Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISS:CAFA.
DR GO; GO:0014807; P:regulation of somitogenesis; IMP:UniProtKB.
DR GO; GO:0001756; P:somitogenesis; ISS:UniProtKB.
DR GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
DR InterPro; IPR017374; Fringe.
DR InterPro; IPR003378; Fringe-like.
DR Pfam; PF02434; Fringe; 1.
DR PIRSF; PIRSF038073; B-acetylgalactosaminyltfrase; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Disease variant;
KW Disulfide bond; Dwarfism; Glycoprotein; Glycosyltransferase;
KW Golgi apparatus; Manganese; Membrane; Metal-binding; Reference proteome;
KW Signal-anchor; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..379
FT /note="Beta-1,3-N-acetylglucosaminyltransferase lunatic
FT fringe"
FT /id="PRO_0000219176"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..379
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 86..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 290
FT /evidence="ECO:0000250"
FT BINDING 129
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT SITE 86..87
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 168..179
FT /evidence="ECO:0000250"
FT DISULFID 197..260
FT /evidence="ECO:0000250"
FT DISULFID 364..373
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..129
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001792"
FT VAR_SEQ 1..73
FT /note="MLKRCGRRLLLALAGALLACLLVLTADPPPPPLPAERGRRALRSLAGPAGAA
FT PAPGLGAAAAAPGALVRDVHS -> MDEQTGRLRLDTYCMSAKQIWAWSKCSGRLWDEH
FT MKWMEGWTDRWTDGWMDGWMDEWSPTPALRSYGGGLSQQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044850"
FT VAR_SEQ 74..144
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044851"
FT VAR_SEQ 130..145
FT /note="LDLLLETWISRHKEMT -> MTPGRCCLAADIQVET (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001793"
FT VAR_SEQ 359..361
FT /note="FRS -> WGN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9187150, ECO:0000303|Ref.5"
FT /id="VSP_001794"
FT VAR_SEQ 362..379
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:9187150, ECO:0000303|Ref.5"
FT /id="VSP_001795"
FT VARIANT 38
FT /note="G -> R"
FT /evidence="ECO:0000269|PubMed:18485326"
FT /id="VAR_046785"
FT VARIANT 188
FT /note="F -> L (in SCDO3; not localized to the correct
FT compartment of the cell; unable to modulate Notch signaling
FT in a cell-based assay; enzymatically inactive;
FT dbSNP:rs104894024)"
FT /evidence="ECO:0000269|PubMed:16385447"
FT /id="VAR_025850"
FT VARIANT 346
FT /note="V -> M (in dbSNP:rs71647813)"
FT /evidence="ECO:0000269|PubMed:18485326"
FT /id="VAR_046786"
FT CONFLICT 104
FT /note="R -> A (in Ref. 5; AAF07187)"
FT /evidence="ECO:0000305"
FT CONFLICT 212
FT /note="R -> L (in Ref. 3; AAC51360)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="R -> L (in Ref. 3; AAC51360)"
FT /evidence="ECO:0000305"
FT CONFLICT 297
FT /note="V -> M (in Ref. 1; BAG53248)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 379 AA; 41773 MW; 4400ECA731B36B45 CRC64;
MLKRCGRRLL LALAGALLAC LLVLTADPPP PPLPAERGRR ALRSLAGPAG AAPAPGLGAA
AAAPGALVRD VHSLSEYFSL LTRARRDAGP PPGAAPRPAD GHPRPLAEPL APRDVFIAVK
TTKKFHRARL DLLLETWISR HKEMTFIFTD GEDEALARHT GNVVITNCSA AHSRQALSCK
MAVEYDRFIE SGRKWFCHVD DDNYVNLRAL LRLLASYPHT RDVYVGKPSL DRPIQAMERV
SENKVRPVHF WFATGGAGFC ISRGLALKMS PWASGGHFMN TAERIRLPDD CTIGYIVEAL
LGVPLIRSGL FHSHLENLQQ VPTSELHEQV TLSYGMFENK RNAVHVKGPF SVEADPSRFR
SIHCHLYPDT PWCPRTAIF
